Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Hepatitis C virus NS2 protein serves as a scaffold for virus assembly by interacting with both structural and nonstructural proteins.

Journal of virology - 1 Jan 2011

Ma Yinghong, Anantpadma Manu, Timpe Jennifer M, Shanmugam Saravanabalaji, Singh Sher M, Lemon Stanley M, Yi Minkyung

Abstract excerpt

Many aspects of the assembly of hepatitis C virus (HCV) remain incompletely understood. To characterize the role of NS2 in the production of infectious virus, we determined NS2 interaction partners among other HCV proteins during productive infection. Pulldown assays showed that NS2 forms complexes with both structural and nonstructural proteins, including E1, E2, p7, NS3, and NS5A. Confocal microscopy also...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cell Line
Share to Hepacivirus

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Mutation

Share to Viral Nonstructural Proteins

Share to Viral Proteins

Share to Viral Structural Proteins

Share to Virus Assembly

Source

Open in PubMed Open full text

Identifiers

PMID: 20962101
DOI: 10.1128/JVI.01070-10
PMCID: PMC3014171

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Hepatitis C virus NS2 protein serves as a scaffold for virus assembly by interacting with both structural and nonstructural proteins.PMID 20962101Read ↗

Structural and functional studies of nonstructural protein 2 of the hepatitis C virus reveal its key role as organizer of virion assembly.Semantic proximity Read ↗

Hepatitis C Virus P7—A Viroporin Crucial for Virus Assembly and an Emerging Target for Antiviral TherapySemantic proximity Read ↗

Structural and functional characterization of nonstructural protein 2 for its role in hepatitis C virus assembly.Semantic proximity Read ↗

The acidic domain of the hepatitis C virus NS4A protein is required for viral assembly and envelopment through interactions with the viral E1 glycoprotein.Semantic proximity Read ↗

NS2 is dispensable for efficient assembly of hepatitis C virus-like particles in a bipartite trans-encapsidation system.Semantic proximity Read ↗

Hepatitis C Virus p7 is Critical for Capsid Assembly and EnvelopmentSemantic proximity Read ↗

The hepatitis C virus NS4B protein can trans-complement viral RNA replication and modulates production of infectious virus.Semantic proximity Read ↗

NS4B self-interaction through conserved C-terminal elements is required for the establishment of functional hepatitis C virus replication complexes.Semantic proximity Read ↗

The amino-terminus of the hepatitis C virus (HCV) p7 viroporin and its cleavage from glycoprotein E2-p7 precursor determine specific infectivity and secretion levels of HCV particle types.Semantic proximity Read ↗

Analysis of hepatitis C virus core/NS5A protein co-localization using novel cell culture systems expressing core-NS2 and NS5A of genotypes 1-7.Semantic proximity Read ↗

Essential role of domain III of nonstructural protein 5A for hepatitis C virus infectious particle assembly.Semantic proximity Read ↗

Proteomics of HCV virions reveals an essential role for the nucleoporin Nup98 in virus morphogenesisSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.